Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P43026 (lipopolysaccharide)
 62,215 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The effect of the addition of (2,6-O-dimethyl)-beta-cyclodextrin (Me beta CD) during growth of Bordetella pertussis in synthetic Stainer-Scholte liquid medium (SS) on lipopolysaccharide (LPS; endotoxin) release was investigated. The Me beta CD concentration used (3 mg/ml) was chosen according to the optimal level found in previous studies to enhance major soluble antigen production. The profiles in SDS-PAGE (sodium dodecyl sulphate/polyacrylamide gel electrophoresis) of LPS extracted from cells grown in SS and SS + Me beta CD media revealed similar patterns. Although the LPS content of whole cells decreased during cell growth, yields obtained at different growth periods in cyclodextrin medium were lower than those corresponding to SS medium alone. Consequently, the level of LPS released in supernatants of both media increased during cellular growth. This amount of free LPS was higher in the cyclodextrin liquid medium and became significant at the beginning of the stationary growth phase. Binding of cyclodextrin to pertussis cells could account for the data obtained. Similar results were obtained with all species of the genus Bordetella.
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PMID:Release of lipopolysaccharide during Bordetella pertussis growth. 821 Jun 77

Bordetella pertussis is composed of a series of active components: (1) a heat-labile or dermonecrotic toxin (HLT); (2) a lipopolysaccharide endotoxin (LPS); (3) pertussis toxin; (4) filamentous hemagglutinin (FHA); (5) agglutinogens; (6) outer membrane proteins; (7) adenylate cyclase; and (8) tracheal cytotoxin. Pertussis toxin (PT), also called lymphocytosis-promoting factor (LPF), encompasses a series of biological activities including: (1) histamine-sensitization (HSF); (2) leukocytosis-promoting activity (LPF); (3) LPF-hemagglutinin (LPF-HA); and (4) pancreatic islet-activating protein (IAP). The heat-labile toxin is inactivated during vaccine production. Pertussis toxin is inactivated when heated to 80 degrees C for 30 min and endotoxin at a temperature greater than 120 degrees C for 30 min. The effect of pre- and post-heat treatment on DTP vaccine, Bordetella pertussis endotoxin, pertussis toxin and a pertussis toxin/endotoxin combination, was determined as related to: (1) paw swelling response; (2) LAL activity (endotoxin); and (3) HSF activity. With the exception of DTP and B. pertussis endotoxin, the average paw swelling response after injection of non-treated and heat-treated test samples was similar to the saline control at all measured time intervals. Contrary to anticipated results, heat treatment enhanced the paw-swelling response of DTP vaccine and B. pertussis endotoxin. Endotoxin levels, as measured by LAL, were significantly lower after heat-treatment, with the exception of B. pertussis endotoxin and the E-1 control. The addition of pertussis toxin, B. pertussis endotoxin or pertussis toxin/endotoxin did not restore LAL values to the levels seen for non-treated DTP vaccine.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Assay of pertussis vaccine reactivity factors by measurement of the paw swelling response, endotoxin and histamine-sensitizing factor. 821 17

We have purified CR3 to homogeneity by affinity chromatography on C3bi-Sepharose and elution with EDTA. C3bi-coated erythrocytes bound to this purified CR3, and binding was dependent on the concentration of both C3bi and CR3, as well as on temperature and the presence of divalent cations. Moreover, binding could be blocked by mAb against CR3 or C3bi and could be enhanced by the addition of integrin modulating factor-1. We used the purified CR3 to test whether several putative ligands of CR3 directly bound the receptor. The interaction of purified CR3 with fibrinogen, filamentous hemagglutinin of Bordetella pertussis, lipophosphoglycan and glycoprotein 63 of Leishmania mexicana, and lipopolysaccharide from Escherichia coli was confirmed. However the interaction of CR3 with zymosan or its major component, beta-glucan, was not observed in these assays. Previous studies showed that binding of C3bi to PMN could be blocked with Arg-Gly-Asp (RGD) containing peptides and were interpreted to indicate that the RGD sequence in C3bi interacts directly with CR3. We found, however, that RGD containing peptides were unable to block the interaction of C3bi with purified CR3, yet retained the ability to block binding of C3bi to cells. We conclude that RGD-peptides do not directly bind CR3, but instead indirectly effect CR3 function. Inasmuch as the effect of RGD-peptides could be mimicked with antibodies against leukocyte response integrin, we suggest that RGD-peptides may bind to leukocyte response integrin on polymorphonuclear leukocytes and influence CR3 activity via this receptor.
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PMID:Ligand specificity of purified complement receptor type three (CD11b/CD18, alpha m beta 2, Mac-1). Indirect effects of an Arg-Gly-Asp (RGD) sequence. 837 80

Spleen cells from the C3H/HeJ mouse strain cannot be stimulated by many smooth-type lipopolysaccharides (LPSs), and by the main biologically-active region (lipid A) of these molecules. The genetic origin of this defect (expression of the mutant allele Lpsd at the chromosome 4 locus) was established over 20 years ago, but its biochemical nature has remained undefined. Several investigators have noted, however, that some particular LPSs can bypass this defect, and stimulate the proliferation of C3H/HeJ B lymphocytes. In this study we compare the mitogenic activities of the LPSs isolated from a wild strain (1414) and from a mutant 'rough' strain (A100) of Bordetella pertussis. Both LPS-1414 and LPS-A100 were mitogenic for C3H/HeJ spleen cells, but their lipid A fragments were not. This indicates that a carbohydrate structure proximal to lipid A is involved in the mitogenic activity. However, the isolated polysaccharides were not mitogenic. Four sugars are common to both LPS-1414 and LPS-A100: an heptose, and three sugars bearing free amino groups. After removal of these four sugars from the LPSs by nitrous acid treatment, the recovered lipooligosaccharides were not mitogenic in Lpsd spleen cells. The results suggest that substructures present in lipid A and in this group of four sugars are both required for induction of a mitogenic effect in Lpsd splenocytes, whereas lipid A alone can stimulate Lpsn spleen cells.
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PMID:Structural features involved in the mitogenic activity of Bordetella pertussis lipopolysaccharides for spleen cells of C3H/HeJ mice. 840 23

Antibody concentrations to three Bordetella pertussis antigens in 94 predisease samples from women who, within a median of 220 days, developed culture-confirmed whooping cough were compared to antibodies in samples from matched controls. The median IgG antibody levels were significantly lower to all three antigens, pertussis toxin, filamentous haemagglutinin and lipopolysaccharide, in the predisease samples of cases as compared to non-cases (p values ranging from 0.0001 to 0.01). A significant difference in antibody distribution was, however, found only to pertussis toxin, measured either by ELISA or by a neutralization test (p values of 0.0004 and 0.007, respectively). The results could be interpreted as meaning that antibodies to the different antigens all participate in protection against disease but that antibodies to pertussis toxin play a major role.
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PMID:Serological correlates in whooping cough. 830 79

Four murine monoclonal antibodies (MAbs) reactive with the outer-core region of the lipopolysaccharide (LPS) from Haemophilus influenzae were generated after immunization with azide-killed H. influenzae RM.7004 AH1-2 and their epitope specificities studied. The monoclonal antibodies: MAHI 6 (IgM), MAHI 5 (IgG2a), MAHI 8 (IgG3), and MAHI 11 (IgG2b) bound to synthetic glycoconjugates or glycolipids with terminal galabiosyl (Gal alpha 1-->4Gal beta 1-) or globotriaosyl (Gal alpha 1-->4Gal beta 1 1-->4GLc) residues as evaluated in enzyme immunoassays (EIA). Glycoconjugates or glycolipids with internally placed galabiose elements were not active, indicating selectively of the MAbs for recognition of the epitope. Nine LPSs from H. influenzae inhibited the binding of the four MAbs. The presence of the galabiosyl disaccharide element in these nine LPSs was evidence by the binding of 125I-labeled Shiga toxin isolated from the bacterium Shigella dysenteriae type 1, reported to have as receptor the Gal alpha 1-->4Gal beta disaccharide (Lindberg et al., J Biol Chem, 1987, 262: 1779-85). Structural studies of these H. influenzae LPSs were also in accord with the presence of the galabiosyl disaccharide, in addition 1H-NMR spectroscopy showed the presence of O-acetyl groups in the RM.7004 AH1-2 LPS. However, differential binding specificities of the MAbs to modified RM.7004 AH1-2 LPSs were observed. MAHI 6 and MAHI 11 bound equally well to LPS, polysaccharides obtained after mild acidic treatment, and dephosphorylated LPS samples as shown in inhibition EIA. In contrast, both dephosphorylated LPS samples and polysaccharides were poorer inhibitors of the binding of MAHI 5 and MAHI 8 to native RM.7004 AH1-2 LPS. Neither the de-O-acylated nor the de-O,N-acylated LPSs were effective inhibitors of any of the four MAbs. These results suggest that the MAbs recognition involves Gal alpha 1-->4Gal and O-acetyl and other saccharide residue(s) from the oligosaccharide moiety of the LPS. The epitopes are also expressed and accessible to recognition in clinical isolates coming from different sources of Neisseria spp., Haemophilus spp., and Moraxella catarrhalis, but not in Bordetella spp., Aeromonas spp. or Enterobacteriaceae as evaluated by whole-bacteria EIA and colony-dot-immunoblotting.
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PMID:Binding specificity for four monoclonal antibodies recognizing terminal Gal alpha 1-->4Gal residues in Haemophilus influenzae lipopolysaccharide. 855 43

Bordetella pertussis lipopolysaccharide (LPS) is biologically active, being both toxic and immunogenic. Using transposon mutagenesis we have identified a genetic locus required for the biosynthesis of LPS in B. pertussis, which has been cloned and sequenced. We have also identified equivalent loci in Bordetella bronchiseptica and Bordetella parapertussis and cloned part of it from B. parapertussis. The amino acid sequences derived from most of the genes present in the sequenced B. pertussis locus are similar to proteins required for the biosynthesis of LPS and other complex polysaccharides from a variety of bacteria. The genes are in a unique arrangement in the locus. Several of the genes identified are similar to genes previously shown to play specific roles in LPS O-antigen biosynthesis. In particular, the amino acid sequence derived from one of the genes is similar to the enzyme encoded by rfbP from Salmonella enterica, which catalyses the transfer of galactose to the undecaprenol phosphate antigen carrier lipid as the first step in building oligosaccharide O-antigen units, which are subsequently assembled to form polymerized O-antigen structures. Defined mutation of this gene in the B. pertussis chromosome results in the inability to express band A LPS, possibly suggesting that the trisaccharide comprising band A is a single O-antigen-like structure and that B. pertussis LPS is similar to semi-rough LPS seen in some mutants of enteric bacteria.
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PMID:The identification, cloning and mutagenesis of a genetic locus required for lipopolysaccharide biosynthesis in Bordetella pertussis. 882 35

Lipooligosaccharides (LOSs) are the major glycolipids expressed on mucosal Gram-negative bacteria, including members of the genera Neisseria, Haemophilus, Bordetella, and Branhamella. They can also be expressed on some enteric bacteria such as Campylobacter jejuni and Campylobacter coli strains. LOS is analogous to the lipopolysaccharide (LPS) found in other Gram-negative families. LOSs share similar lipid A structures with an identical array of functional activities as LPSs. LOSs lack O-antigen units with the LOS oligosaccharide structures limited to 10 saccharide units. The LOS species of pathogenic Neisseria can play a major role in pathogenesis through enhancing the resistance of the organism to killing by normal human serum. Other distinguishing characteristics of LOS are the structural and antigenic similarity of some LOS species to human glycolipids and the potential for certain LOSs to be modified in vivo by host substances or secretions. These modifications of LOS in different environments of the host result in synthesis of new LOS structures that probably benefit the survival of the pathogen. The LOS of N. gonorrhoeae can act as a ligand of human receptors, promoting invasion of host cells. It is becoming clearer that LOSs are crucial factors in the pathogenesis of bacteria that express them.
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PMID:The lipooligosaccharides of pathogenic gram-negative bacteria. 889 99

The tetrameric repeat units 5'-CAAT-3' and 5'-GCAA-3' are associated with phase variable expression of lipopolysaccharide biosynthetic genes in Haemophilus influenzae. Four other tetrameric repeat units have also been reported from H. influenzae strain Rd, 5'-CAAC-3', 5'-GACA-3', 5'-AGCT-3', and 5'-TTTA-3', which are also associated with putative virulence factors. Using oligonucleotide probes corresponding to five tandem copies of each of these tetramers, we have screened three strains of Neisseria meningitidis and one each of Neisseria gonorrhoeae, Neisseria lactamica, Haemophilus parainfluenzae, Bordetella pertussis, Bordetella parapertussis, Bordetella bronchiceptica and Moraxella catarrhalis for the presence of these motifs. We have demonstrated the presence of multiple copies of the 5'-GCAA-3' motif in all the Neisseria strains tested, and also the repeated motif 5'-CAAC-3' in M. catarrhalis. We have further demonstrated by Southern blot analysis that the 5'-CAAC-3' repeats detected in M. catarrhalis are probably associated with the same genes as in H. influenzae, but that the 5'-GCAA-3' motifs in N. meningitidis are not. The use of characterised tetrameric DNA sequences as hybridisation probes may prove useful in the identification of novel phase variable virulence determinants in organisms other than H. influenzae.
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PMID:Tetrameric repeat units associated with virulence factor phase variation in Haemophilus also occur in Neisseria spp. and Moraxella catarrhalis. 893 64

Three hybridomas (P1P3, D7 and 60.5) producing monoclonal antibodies (mAbs) against Bordetella pertussis lipopolysaccharide (LPS) were established. All reacted with the LPS from a typical, vaccine strain of B. pertussis (1414), but not with that of a variant strain (A100). Two of these mAbs (P1P3 and 60.5) cross-reacted with a B. bronchiseptica LPS; only one (P1P3) reacted with a B. parapertussis LPS. ELISA reactivities with intact LPSs, and defined partial structures covalently linked to bovine serum albumin, were compared. mAb 60.5 bound to the terminal region of a distal trisaccharide consisting of N-acetylated amino sugars. D7 reacted with a substructure which can be modified in the B. parapertussis and B. bronchiseptica LPSs by addition of a polymeric O-chain. P1P3 bound to a nonacetylated glucosamine substituted with L-glycero-D-manno-heptose, present in the 'core' of the B. pertussis LPS. These mAbs may be useful for rapid typing of Bordetella in clinical isolates.
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PMID:Epitopes of Bordetella pertussis lipopolysaccharides as potential markers for typing of isolates with monoclonal antibodies. 893 24


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